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Vol. 13, No. 19, pp. 2514-2526, October 1, 1999
Department of Cell and Cancer Biology, Medicine Branch, Division of
Clinical Sciences, National Cancer Institute, National Institutes of
Health, Bethesda, Maryland 20892 USA
Although the molecular mechanisms of TNF signaling have been largely
elucidated, the principle that regulates the balance of life and death
is still unknown. We report here that the death domain kinase RIP, a
key component of the TNF signaling complex, was cleaved by Caspase-8 in
TNF-induced apoptosis. The cleavage site was mapped to the aspartic
acid at position 324 of RIP. We demonstrated that the cleavage of RIP
resulted in the blockage of TNF-induced NF-
B activation. RIPc, one
of the cleavage products, enhanced interaction between TRADD and
FADD/MORT1 and increased cells' sensitivity to TNF. Most
importantly, the Caspase-8 resistant RIP mutants protected cells
against TNF-induced apopotosis. These results suggest that cleavage of
RIP is an important process in TNF-induced apoptosis. Further more, RIP
cleavage was also detected in other death receptor-mediated apoptosis.
Therefore, our study provides a potential mechanism to convert cells
from life to death in death receptor-mediated apoptosis.
[Key Words:
TNF; apoptosis; NF-B; RIP; caspase]
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